BMRB Entry 31234

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31234
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Intermediate state of Src kinase domain
Deposition date:
2025-03-15
Original release date:
2026-01-18
Authors:
Cui, Y.; Ali, R.; Clay, M.; Rossi, P.; Liu, A.; Yang, D.; Gough, N.; Geiger, T.; Kalodimos, C.
Citation:

Citation: Cui, Y.; Ali, R.; Clay, M.; Rossi, P.; Liu, A.; Yang, D.; Gough, N.; Geiger, T.; Kalodimos, C.. "Intermediate state of Src kinase domain"  .

Assembly members:

Assembly members:
entity_1, polymer, 286 residues, 32739.637 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SKPQTQGLAKDAWEIPRESL RLEVKLGQGCFGEVWMGTWN GTTRVAIKTLKPGTMSPEAF LQEIQVMKKLRHEKLVQLYA VVSEEPIYIVTEYMSKGSLL DFLKGETGKYLRLPQLVDMA AQIASGMAYVERMNYVHRDL RAANILVGENLVCKVADFGL ARLIEDNEYTARQGAKFPIK WTAPEAALYGRFTIKSDVWS FGILLTELTTKGRVPYPGMV NREVLDQVERGYRMPCPPEC PESLHDLMCQCWRKEPEERP TFEYLQAFLEDYFTSTEPQY QPGENL

Data sets:
Data typeCount
13C chemical shifts841
15N chemical shifts445
1H chemical shifts997

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 286 residues - 32739.637 Da.

1   SERLYSPROGLNTHRGLNGLYLEUALALYS
2   ASPALATRPGLUILEPROARGGLUSERLEU
3   ARGLEUGLUVALLYSLEUGLYGLNGLYCYS
4   PHEGLYGLUVALTRPMETGLYTHRTRPASN
5   GLYTHRTHRARGVALALAILELYSTHRLEU
6   LYSPROGLYTHRMETSERPROGLUALAPHE
7   LEUGLNGLUILEGLNVALMETLYSLYSLEU
8   ARGHISGLULYSLEUVALGLNLEUTYRALA
9   VALVALSERGLUGLUPROILETYRILEVAL
10   THRGLUTYRMETSERLYSGLYSERLEULEU
11   ASPPHELEULYSGLYGLUTHRGLYLYSTYR
12   LEUARGLEUPROGLNLEUVALASPMETALA
13   ALAGLNILEALASERGLYMETALATYRVAL
14   GLUARGMETASNTYRVALHISARGASPLEU
15   ARGALAALAASNILELEUVALGLYGLUASN
16   LEUVALCYSLYSVALALAASPPHEGLYLEU
17   ALAARGLEUILEGLUASPASNGLUTYRTHR
18   ALAARGGLNGLYALALYSPHEPROILELYS
19   TRPTHRALAPROGLUALAALALEUTYRGLY
20   ARGPHETHRILELYSSERASPVALTRPSER
21   PHEGLYILELEULEUTHRGLULEUTHRTHR
22   LYSGLYARGVALPROTYRPROGLYMETVAL
23   ASNARGGLUVALLEUASPGLNVALGLUARG
24   GLYTYRARGMETPROCYSPROPROGLUCYS
25   PROGLUSERLEUHISASPLEUMETCYSGLN
26   CYSTRPARGLYSGLUPROGLUGLUARGPRO
27   THRPHEGLUTYRLEUGLNALAPHELEUGLU
28   ASPTYRPHETHRSERTHRGLUPROGLNTYR
29   GLNPROGLYGLUASNLEU

Samples:

sample_1: SrcA311I kinase, [U-13C; U-15N; U-2H], 250 uM; potassium chloride 25 mM; sodium chloride 500 mM; BME 3 mM; EDTA 1 mM

sample_2: SrcA311I kinase, [U-15N; U-2H] ILVMAT CH3 FY CEHE, 250 uM; potassium chloride 25 mM; sodium chloride 500 mM; BME 3 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 500 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D CCH_Noesysample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin, Bruker Biospin - collection

PSVS, Bhattacharya and Montelione - geometry optimization

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz
  • Bruker AVANCE NEO 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks